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Crystal structure of a plasmid partition protein from borrelia burgdorferi at 2.25A resolution

Analyse Crystal structure of a plasmid partition protein from borrelia burgdorferi at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K9H
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pf-32 protein
UniProt: O68233
Ligands: SO4
Pockets: 7 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pf-32 protein	protein	229	41% helix, 19% strand	O68233

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.69	0.88	28	empty
2	51	0.65	0.95	15	empty
3	221	0.57	0.79	36	SO4
4	104	0.54	0.84	33	empty
5	100	0.46	0.79	23	empty

Interfaces

1 interface between chains.

A–B · 1163 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3K9H · Crystal structure of a plasmid partition protein from borrelia burgdorferi at 2.25A… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O68233
Elsewhere: RCSB PDB 3K9H · PDBe 3K9H · UniProt O68233

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